ID A0A3Q0KRZ6_SCHMA Unreviewed; 736 AA.
AC A0A3Q0KRZ6; A0A3Q0KS14;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Propionyl-CoA carboxylase alpha chain, mitochondrial {ECO:0000256|ARBA:ARBA00018058};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
DE AltName: Full=Propanoyl-CoA:carbon dioxide ligase subunit alpha {ECO:0000256|ARBA:ARBA00031557};
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183 {ECO:0000313|WBParaSite:Smp_165400.3};
RN [1] {ECO:0000313|Proteomes:UP000008854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN [2] {ECO:0000313|WBParaSite:Smp_165400.1, ECO:0000313|WBParaSite:Smp_165400.3}
RP IDENTIFICATION.
RC STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_165400.1,
RC ECO:0000313|WBParaSite:Smp_165400.3};
RG WormBaseParasite;
RL Submitted (DEC-2018) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoyl-CoA + hydrogencarbonate = (2S)-ethylmalonyl-CoA
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:59520, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:60909, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001715};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59521;
CC Evidence={ECO:0000256|ARBA:ARBA00001715};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-
CC CoA + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23720,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456216; EC=6.4.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000634};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC Evidence={ECO:0000256|ARBA:ARBA00000634};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000256|ARBA:ARBA00005060}.
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DR AlphaFoldDB; A0A3Q0KRZ6; -.
DR STRING; 6183.A0A3Q0KRZ6; -.
DR EnsemblMetazoa; Smp_165400.1; Smp_165400.1; Smp_165400.
DR EnsemblMetazoa; Smp_165400.3; Smp_165400.3; Smp_165400.
DR WBParaSite; Smp_165400.1; Smp_165400.1; Smp_165400.
DR WBParaSite; Smp_165400.3; Smp_165400.3; Smp_165400.
DR InParanoid; A0A3Q0KRZ6; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.30; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR041265; PCC_BT.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF18140; PCC_BT; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000008854};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 46..493
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 165..362
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 652..735
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 736 AA; 81862 MW; DC0794FFBD434075 CRC64;
MYLVLQSCQT RIGFRGSITI FRRLSTPVCF HREFYWNDRC DNNEEKFEKV LIANRGEIAC
RIIQSCKRLG IRTVAIHSEA DYLSRFVSMA DEAVCVGPSP SAQSYLNISA ILNAVKSTSA
QAVHPGYGFL SENTLFAAEL EKMNVVFLGP NSRAIKAMGD KIESKRIANQ AKVNCIPGYD
GEVDGPDEAA RIAAEIGYPV MIKASTGGGG KGMRIAWDEK EVREGYRLSK SEAKASFGDD
RMLIEKFIDN PRHIEIQLLC DRHGNAIYLN ERECSIQRRN QKVIEEAPST FLDSGLRKAM
GEQAVSLAKA VNYDSAGTVE FLVDSKRNFY FLEMNTRLQV EHPITECITG VDIVHQMLRV
GKGHPLMLSQ SDIPVNGWAF ECRVYAEDPY KAFGLPSIGR LRTYSEPLHI PNVCCDSGVN
EGSEISIYYD PMICKLVTYG PDRQTALNTM TKALDSYVIR GVTHNIPLLR DIVTEKRFVS
GDISTKYLSE VYPDGFKGKV LDQKELDTLI SVSASIFAKN DARIRNCSGE SQWDLVASLN
ENSANSDPKS RSYIRCIVTR DCSGFQVRMS PWEPPKHINQ QDVHITSQSS KSQESLVRVA
DNFKLSDKII NHSYDGNEVI LQLLDKSINT VCLQYLGTAF PVEIMNTTAA WFRAAYMPPP
RVIDYGSICI APMPGLVRSI AVKVGDRVGE GQELCILEAM KMQNSLTASR SGVIKKVNFK
AGGSVSEGDI LVELEK
//
